IDENTIFICATION OF THE SIDEROPHORES FROM VIBRIO-HOLLISAE AND VIBRIO-MIMICUS AS AEROBACTIN

IDENTIFICATION OF THE SIDEROPHORES FROM VIBRIO-HOLLISAE AND VIBRIO-MIMICUS AS AEROBACTIN
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DOI:
10.1111/j.1574-6968.1994.tb06824.x
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发表时间:
1994-05-01
影响因子:
2.1
通讯作者:
YAMAMOTO, S
YAMAMOTO, S
中科院分区:
生物学4区
文献类型:
--
作者:
OKUJO, N;YAMAMOTO, S

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从霍利氏弧菌ATCC 33564和拟态弧菌ATCC 33653的低铁培养物中提纯了羟甲酸铁载体。结合H-1和C-13核磁共振波谱、快原子轰击质谱仪和成分分析,确定这两个铁载体均为好氧蛋白,是一种以柠檬酸为基础的二羟基己二酸酯类铁载体,在肠杆菌科物种中广泛存在。属于这些物种的另外四株临床菌株也产生需氧菌素。作为对铁限制的反应,所有菌株都表达了两个高分子质量的外膜蛋白。表观分子量为77 kDa的蛋白质可能是铁好氧肌动蛋白受体,这是所有菌株所共有的。
Hydroxamate siderophores were purified from low-iron cultures of Vibrio hollisae ATCC 33564 and Vibrio mimicus ATCC 33653. By a combination of H-1 and C-13 NMR spectroscopy, fast atom bombardment mass spectrometry, and compositional analysis, both of the siderophores were identified as aerobactin, a citrate-based dihydroxamate siderophore, which is highly prevalent in species of the family Enterobacteriaceae. Four other clinical strains belonging to these species also produced aerobactin. In response to iron limitation, all strains expressed two high molecular mass outer membrane proteins. The protein with an apparent molecular mass of 77 kDa, which was common to all strains examined, may be the ferric aerobactin receptor.